ID   A0A086Z1P0_9BIFI        Unreviewed;       477 AA.
AC   A0A086Z1P0;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   SubName: Full=D-alanyl-D-alanine carboxypeptidase/D-alanyl-D-alanine-endopeptidase {ECO:0000313|EMBL:KFI40440.1};
DE            EC=3.4.16.4 {ECO:0000313|EMBL:KFI40440.1};
GN   ORFNames=BACT_1144 {ECO:0000313|EMBL:KFI40440.1};
OS   Bifidobacterium actinocoloniiforme DSM 22766.
OC   Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; Bifidobacterium.
OX   NCBI_TaxID=1437605 {ECO:0000313|EMBL:KFI40440.1, ECO:0000313|Proteomes:UP000029015};
RN   [1] {ECO:0000313|EMBL:KFI40440.1, ECO:0000313|Proteomes:UP000029015}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22766 {ECO:0000313|EMBL:KFI40440.1,
RC   ECO:0000313|Proteomes:UP000029015};
RA   Ventura M., Milani C., Lugli G.A.;
RT   "Genomics of Bifidobacteria.";
RL   Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase S13 family.
CC       {ECO:0000256|ARBA:ARBA00006096}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KFI40440.1}.
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DR   EMBL; JGYK01000001; KFI40440.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A086Z1P0; -.
DR   STRING; 1437605.AB656_04320; -.
DR   eggNOG; COG2027; Bacteria.
DR   Proteomes; UP000029015; Unassembled WGS sequence.
DR   GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 2.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
DR   InterPro; IPR000667; Peptidase_S13.
DR   NCBIfam; TIGR00666; PBP4; 1.
DR   PANTHER; PTHR30023; D-ALANYL-D-ALANINE CARBOXYPEPTIDASE; 1.
DR   PANTHER; PTHR30023:SF0; PENICILLIN-SENSITIVE CARBOXYPEPTIDASE A; 1.
DR   Pfam; PF02113; Peptidase_S13; 2.
DR   PRINTS; PR00922; DADACBPTASE3.
DR   SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
PE   3: Inferred from homology;
KW   Carboxypeptidase {ECO:0000313|EMBL:KFI40440.1};
KW   Hydrolase {ECO:0000313|EMBL:KFI40440.1};
KW   Protease {ECO:0000313|EMBL:KFI40440.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029015}.
FT   REGION          236..261
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   477 AA;  48415 MW;  42DEA88DCDA850DA CRC64;
     MRGPQRHVAR TLLAAGLVVV AFAGYVAADI ADLVPGPLTR DARPSQGQAA GPAQAWAPAR
     VAGDLETGRG VDAAAAQGVI DTFAATPGLG SDYSVLIADA DGTVAAERDQ ENLRQPASTL
     KTLTAAAAAG SLDMGSTIPT EAYLSQSAGA GAKLTLKGQG DMLLGPGASD PNHVNGRAGL
     GTLAQETAQV LKARSISKVS LAYDAGKFGS VRSSQGIEAN NPGGVYFTPT SAMAVDEGRQ
     RSPQDRDAAP DAAGVYVPHD QDPEGQAARV FAQRLREQGI DLEGEPSAGQ AAQADQPLAQ
     VQSAPLIQIM AYMLRTSDNT LAELFGRLTA IKEGKENSPE GAVQAVGQAL EREGIKLEGG
     AHMADCSGLS PGSQVSVTTL AAVQRLACDG RHGRLAPLVE GLSVAGLVGT AANRGRGPAS
     GLARVKTGSL DQVTAMTGNV SRTRGGLLVF AVIVNNPSDM GAAVKAVDTL LSGLPQL
//